HYALP_MOUSE
ID HYALP_MOUSE Reviewed; 512 AA.
AC P48794; Q7TSD6; Q812F4; Q9DAQ1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Hyaluronidase PH-20;
DE Short=Hyal-PH20;
DE EC=3.2.1.35;
DE AltName: Full=Hyaluronoglucosaminidase PH-20;
DE AltName: Full=Sperm adhesion molecule 1;
DE AltName: Full=Sperm surface protein PH-20;
DE Flags: Precursor;
GN Name=Spam1; Synonyms=Ph20, Spam;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Sperm;
RA Ramarao C.S., Primakoff P.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Testis;
RX PubMed=12065596; DOI=10.1074/jbc.m204596200;
RA Baba D., Kashiwabara S., Honda A., Yamagata K., Wu Q., Ikawa M., Okabe M.,
RA Baba T.;
RT "Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the
RT layer of cumulus cells and fertilize the egg.";
RL J. Biol. Chem. 277:30310-30314(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RA Hardy C.M., Mobbs K.J.;
RT "Assessment of contraceptive vaccines based on mouse sperm protein PH-20
RT (SPAM-1).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7794889; DOI=10.1021/bi00024a002;
RA Thaler C.D., Cardullo R.A.;
RT "Biochemical characterization of a glycosylphosphatidylinositol-linked
RT hyaluronidase on mouse sperm.";
RL Biochemistry 34:7788-7795(1995).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in sperm-egg adhesion. Upon fertilization sperm must
CC first penetrate a layer of cumulus cells that surrounds the egg before
CC reaching the zona pellucida. The cumulus cells are embedded in a matrix
CC containing hyaluronic acid which is formed prior to ovulation. This
CC protein aids in penetrating the layer of cumulus cells by digesting
CC hyaluronic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
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DR EMBL; U33958; AAA76603.1; -; mRNA.
DR EMBL; AB085677; BAC55070.1; -; Genomic_DNA.
DR EMBL; AY228460; AAP49832.1; -; mRNA.
DR EMBL; AK005638; BAB24161.1; -; mRNA.
DR CCDS; CCDS19947.1; -.
DR RefSeq; NP_001073344.1; NM_001079875.2.
DR RefSeq; NP_033267.2; NM_009241.3.
DR RefSeq; XP_006505088.1; XM_006505025.2.
DR AlphaFoldDB; P48794; -.
DR SMR; P48794; -.
DR BioGRID; 203421; 1.
DR STRING; 10090.ENSMUSP00000031693; -.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; P48794; 4 sites.
DR PaxDb; P48794; -.
DR PeptideAtlas; P48794; -.
DR PRIDE; P48794; -.
DR ProteomicsDB; 269512; -.
DR DNASU; 20690; -.
DR Ensembl; ENSMUST00000031693; ENSMUSP00000031693; ENSMUSG00000029682.
DR Ensembl; ENSMUST00000202331; ENSMUSP00000143944; ENSMUSG00000029682.
DR Ensembl; ENSMUST00000202569; ENSMUSP00000143970; ENSMUSG00000029682.
DR GeneID; 20690; -.
DR KEGG; mmu:20690; -.
DR UCSC; uc009bby.2; mouse.
DR CTD; 6677; -.
DR MGI; MGI:109335; Spam1.
DR VEuPathDB; HostDB:ENSMUSG00000029682; -.
DR eggNOG; ENOG502R6HD; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR InParanoid; P48794; -.
DR OMA; DDQASCE; -.
DR OrthoDB; 1096692at2759; -.
DR PhylomeDB; P48794; -.
DR TreeFam; TF321598; -.
DR BioGRID-ORCS; 20690; 1 hit in 71 CRISPR screens.
DR PRO; PR:P48794; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P48794; protein.
DR Bgee; ENSMUSG00000029682; Expressed in spermatid and 8 other tissues.
DR Genevisible; P48794; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro.
DR GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR InterPro; IPR001439; Hyaluronidase_PH20/Hyal5.
DR PANTHER; PTHR11769; PTHR11769; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000250"
FT CHAIN 36..?
FT /note="Hyaluronidase PH-20"
FT /id="PRO_0000012093"
FT PROPEP ?..512
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012094"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..351
FT /evidence="ECO:0000250"
FT DISULFID 223..237
FT /evidence="ECO:0000250"
FT DISULFID 376..387
FT /evidence="ECO:0000250"
FT DISULFID 381..435
FT /evidence="ECO:0000250"
FT DISULFID 437..464
FT /evidence="ECO:0000250"
FT CONFLICT 182
FT /note="E -> R (in Ref. 1; AAA76603)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="F -> L (in Ref. 1; AAA76603)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="N -> H (in Ref. 2; BAC55070)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="H -> R (in Ref. 4; BAB24161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58498 MW; 6502F9FC75E7C86F CRC64;
MGELRFKHLF WGSFVESGGT FQTVLIFLLI PCSLTVDYRA APILSNTTFL WIWNVPTERC
VGNVNDPIDL SFFSLIGSPR KTATGQPVTL FYVDRLGLYP HIDANQAEHY GGIPQRGDYQ
AHLRKAKTDI EHYIPDDKLG LAIIDWEEWR PTWLRNWKPK DNYRNKSIEL VQSTNPGLSI
TEATQKAIQQ FEEAGRKFME GTLHLGKFLR PNQLWGYYLF PDCYNNKFQD PKYDGQCPAV
EKKRNDNLKW LWKASTGLYP SVYLKKDLKS NRQATLYVRY RVVEAIRVSK VGNASDPVPI
FVYIRLVFTD RTSEYLLEDD LVNTIGEIVA LGTSGIIIWD AMSLAQRAAG CPILHKYMQT
TLNPYIVNVT LAAKMCSQTL CNEKGMCSRR KESSDVYLHL NPSHFDIMLT ETGKYEVLGN
PRVGDLEYFS EHFKCSCFSR MTCKETSDVK NVQDVNVCVG DNVCIKAKVE PNPAFYLLPG
KSLLFMTTLG HVLYHLPQDI FVFPRKTLVS TP
